Human cytidine triphosphate synthetase 1 interacting proteins

被引：10

作者：

Higgins, M. J. ^{[1
]}

Loiselle, D. ^{[2
]}

Haystead, T. A. ^{[2
]}

Graves, L. M. ^{[1
]}

机构：

[1] Univ N Carolina, Dept Pharmacol, Chapel Hill, NC 27599 USA

[2] Duke Univ, Dept Pharmacol & Canc Biol, Raleigh, NC USA

来源：

NUCLEOSIDES NUCLEOTIDES & NUCLEIC ACIDS | 2008年 / 27卷 / 6-7期

关键词：

CTP; CTP synthetase; tubulin; Pin1; localization;

D O I：

10.1080/15257770802146502

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We investigated the interacting proteins and intracellular localization of CTP synthetase 1 (CTPS1) in mammalian cells. CTPS1 interacted with a GST- peptidyl prolyl isomerase, Pin1 fusion (GST-Pin1) in a Ser 575 (S575) phosphorylation-dependent manner. Immunoprecipitation experiments demonstrated that CTPS1 also bound tubulin, and thirteen additional coimmunoprecipitating proteins were identified by mass spectrometry. Immunolocalization experiments showed that tubulin and CTPS1 colocalized subcellularly. Taxol treatment enhanced this but cotreatment of cells with the CTPS inhibitor, cyclopentenyl cytosine (CPEC), and taxol failed to disrupt the colocalization. Thus, these studies provide novel information on the potential interacting proteins that may regulate CTPS1 function or intracellular localization.

引用

页码：850 / 857

页数：8

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